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Database: UniProt
Entry: A0A091R520_9GRUI
LinkDB: A0A091R520_9GRUI
Original site: A0A091R520_9GRUI 
ID   A0A091R520_9GRUI        Unreviewed;       959 AA.
AC   A0A091R520;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=A-kinase anchor protein 13 {ECO:0000313|EMBL:KFQ34606.1};
DE   Flags: Fragment;
GN   ORFNames=N332_05808 {ECO:0000313|EMBL:KFQ34606.1};
OS   Mesitornis unicolor (brown roatelo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX   NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ34606.1, ECO:0000313|Proteomes:UP000053369};
RN   [1] {ECO:0000313|EMBL:KFQ34606.1, ECO:0000313|Proteomes:UP000053369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ34606.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; KK809617; KFQ34606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091R520; -.
DR   Proteomes; UP000053369; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13392; PH_AKAP13; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041020; PH_16.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR13944:SF18; A-KINASE ANCHOR PROTEIN 13; 1.
DR   PANTHER; PTHR13944; AGAP007712-PA; 1.
DR   Pfam; PF17838; PH_16; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KFQ34606.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053369};
KW   Transferase {ECO:0000313|EMBL:KFQ34606.1}.
FT   DOMAIN          150..347
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          387..489
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          831..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          723..757
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..912
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ34606.1"
FT   NON_TER         959
FT                   /evidence="ECO:0000313|EMBL:KFQ34606.1"
SQ   SEQUENCE   959 AA;  110189 MW;  E42BE8E49E02DC1B CRC64;
     FQPQKGVLQA HDTSSLSTVT MRNKSSQPKE RPRSAILAPD ENTVTSIFNN RRSQQPTALS
     KSVSIQNIAG VGNDDNLINT WKFLSQSTDS LNKISRVNES TESLVDEGAD MNEGQLMGDL
     EFDSKQLEAE SWSQVVDTKF LQQQNKDVVM RQDVIYELMQ TEMHHVRTLK IMNDVYSAGM
     LKELQYDQQV VDKIFPCLEN LLHIHSHFFQ RILERKKESL ADKNEKNFVI KRIGDVLVNQ
     FSGESAERMK KTYGKFCGHH NEAVNNFKDL YSKDKRFQAF VKKKMSSSLV RRLGISECIL
     LVTQRITKYP VLLQRILQYT KENEVEHEDL TQALNLIKDM IAAVNNKVSN YEKKMRLSEI
     YNRTDSKSIM RMKSGQMFAR EDLRHRKLIR DGPVSLKNAA GRLKEVQAVL LSDVLVFLQE
     KDQKYVFPSL DQKSTVISLK KLIVREVAHE EKGLFLISMG VKDPEMVEVH ASSKEERNSW
     IQIIQDTMNT MDRDEDEGVP CESEFEKKVS DAKVRGLKEQ LQQKDKQILL LLEEKAKIFR
     DMADSSVQEE MPGSRLLFRA NTEEAPKGEA IMKTAINEVE LLQDLVNRSL GTALGQQVSS
     AALEQEGGVG PISLPRRAET FGGFDSHQMN ASKCGAKDEG DEAQDLRRTE SDSILKKGGN
     ANLMFMLKRN NEQVLQTITS LHKLLSALQG VVLQQDTYIE DQKLALSERA LTRSFFRPTS
     LLEQEKQRNL EKQRQELANL KKQQMQHQEE RRKREKEWEV REKELAEKEA HLAQREEQVQ
     KGWQDLERER EELQVKKASY QLDLERLRSA QKQLEREKAQ FKQDMEQLAQ MQQEPDHNQL
     SNLHEKLARI PSQSSTDDSS KQKSPSLPKQ GHFDAELSVS PKRNSLSRTH KEKSTFHLLS
     TINQTNKAAE EQPQMPTRLF SLAKPKEKKE KKKKGRGHRS QQSDSHSSEA PPEGEEIFC
//
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